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P99024 (TBB5_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tubulin beta-5 chain
Gene names
Name:Tubb5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length444 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tubulin is the major constituent of microtubules. It binds two moles of GTP, one at an exchangeable site on the beta chain and one at a non-exchangeable site on the alpha chain.

Subunit structure

Interacts with MX1 By similarity. Dimer of alpha and beta chains. A typical microtubule is a hollow water-filled tube with an outer diameter of 25 nm and an inner diameter of 15 nM. Alpha-beta heterodimers associate head-to-tail to form protofilaments running lengthwise along the microtubule wall with the beta-tubulin subunit facing the microtubule plus end conferring a structural polarity. Microtubules usually have 13 protofilaments but different protofilament numbers can be found in some organisms and specialized cells. Interacts with PIFO. May interact with RNABP10. Ref.8 Ref.10

Subcellular location

Cytoplasmcytoskeleton.

Tissue specificity

Ubiquitously expressed with highest levels in spleen, thymus and immature brain.

Post-translational modification

Some glutamate residues at the C-terminus are either polyglutamylated or polyglycylated. These 2 modifications occur exclusively on glutamate residues and result in either polyglutamate or polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Both modifications can coexist on the same protein on adjacent residues, and lowering polyglycylation levels increases polyglutamylation, and reciprocally. The precise function of such modifications is still unclear but they are regulate the assembly and dynamics of axonemal microtubules.

Sequence similarities

Belongs to the tubulin family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 444444Tubulin beta-5 chain
PRO_0000048246

Regions

Nucleotide binding140 – 1467GTP Potential

Amino acid modifications

Modified residue581N6-acetyllysine; alternate Ref.11
Modified residue581N6-succinyllysine; alternate Ref.11
Modified residue1721Phosphoserine; by CDK1 By similarity
Modified residue3181Omega-N-methylarginine By similarity
Cross-link58Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate By similarity
Cross-link324Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity

Experimental info

Sequence conflict151Q → P in BAB27292. Ref.2
Sequence conflict1141D → N in BAE40217. Ref.2
Sequence conflict1431T → N in BAE28709. Ref.2
Sequence conflict2641H → D in BAE40217. Ref.2
Sequence conflict3071H → N in BAE39835. Ref.2
Sequence conflict3571P → T in BAE40217. Ref.2
Sequence conflict4001G → A in AAA40510. Ref.6

Sequences

Sequence LengthMass (Da)Tools
P99024 [UniParc].

Last modified August 13, 1987. Version 1.
Checksum: 1E6CD0A36773A103

FASTA44449,671
        10         20         30         40         50         60 
MREIVHIQAG QCGNQIGAKF WEVISDEHGI DPTGTYHGDS DLQLDRISVY YNEATGGKYV 

        70         80         90        100        110        120 
PRAILVDLEP GTMDSVRSGP FGQIFRPDNF VFGQSGAGNN WAKGHYTEGA ELVDSVLDVV 

       130        140        150        160        170        180 
RKEAESCDCL QGFQLTHSLG GGTGSGMGTL LISKIREEYP DRIMNTFSVV PSPKVSDTVV 

       190        200        210        220        230        240 
EPYNATLSVH QLVENTDETY CIDNEALYDI CFRTLKLTTP TYGDLNHLVS ATMSGVTTCL 

       250        260        270        280        290        300 
RFPGQLNADL RKLAVNMVPF PRLHFFMPGF APLTSRGSQQ YRALTVPELT QQVFDAKNMM 

       310        320        330        340        350        360 
AACDPRHGRY LTVAAVFRGR MSMKEVDEQM LNVQNKNSSY FVEWIPNNVK TAVCDIPPRG 

       370        380        390        400        410        420 
LKMAVTFIGN STAIQELFKR ISEQFTAMFR RKAFLHWYTG EGMDEMEFTE AESNMNDLVS 

       430        440 
EYQQYQDATA EEEEDFGEEA EEEA 

« Hide

References

« Hide 'large scale' references
[1]"The mammalian beta-tubulin repertoire: hematopoietic expression of a novel, heterologous beta-tubulin isotype."
Wang D., Villasante A., Lewis S.A., Cowan N.J.
J. Cell Biol. 103:1903-1910(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J and DBA/2.
Tissue: Bone marrow, Embryo, Kidney, Liver, Pituitary, Placenta, Spinal ganglion, Spleen, Sympathetic ganglion and Thymus.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]Lubec G., Kang S.U., Klug S., Yang J.W., Zigmond M.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 3-19; 63-121; 163-174; 217-241; 242-276; 283-297; 310-318; 321-359 AND 381-390, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: C57BL/6.
Tissue: Brain and Hippocampus.
[6]"Five mouse tubulin isotypes and their regulated expression during development."
Lewis S.A., Lee M.G.-S., Cowan N.J.
J. Cell Biol. 101:852-861(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 325-444.
[7]"Tubulin polyglutamylase enzymes are members of the TTL domain protein family."
Janke C., Rogowski K., Wloga D., Regnard C., Kajava A.V., Strub J.-M., Temurak N., van Dijk J., Boucher D., van Dorsselaer A., Suryavanshi S., Gaertig J., Edde B.
Science 308:1758-1762(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYGLUTAMYLATION.
[8]"RanBP10 is a cytoplasmic guanine nucleotide exchange factor that modulates noncentrosomal microtubules."
Schulze H., Dose M., Korpal M., Meyer I., Italiano J.E. Jr., Shivdasani R.A.
J. Biol. Chem. 283:14109-14119(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH RANBP10.
[9]"Evolutionary divergence of enzymatic mechanisms for posttranslational polyglycylation."
Rogowski K., Juge F., van Dijk J., Wloga D., Strub J.-M., Levilliers N., Thomas D., Bre M.-H., Van Dorsselaer A., Gaertig J., Janke C.
Cell 137:1076-1087(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: POLYGLYCYLATION.
[10]"Pitchfork regulates primary cilia disassembly and left-right asymmetry."
Kinzel D., Boldt K., Davis E.E., Burtscher I., Trumbach D., Diplas B., Attie-Bitach T., Wurst W., Katsanis N., Ueffing M., Lickert H.
Dev. Cell 19:66-77(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PIFO.
[11]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-58, SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-58, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic fibroblast.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04663 mRNA. Translation: CAA28369.1.
AK010960 mRNA. Translation: BAB27292.1.
AK011263 mRNA. Translation: BAB27504.1.
AK051164 mRNA. Translation: BAC34541.1.
AK051393 mRNA. Translation: BAC34623.1.
AK083327 mRNA. Translation: BAC38866.1.
AK146567 mRNA. Translation: BAE27265.1.
AK148978 mRNA. Translation: BAE28709.1.
AK151215 mRNA. Translation: BAE30210.1.
AK151670 mRNA. Translation: BAE30596.1.
AK160225 mRNA. Translation: BAE35700.1.
AK161575 mRNA. Translation: BAE36471.1.
AK165249 mRNA. Translation: BAE38103.1.
AK167691 mRNA. Translation: BAE39738.1.
AK167779 mRNA. Translation: BAE39811.1.
AK167808 mRNA. Translation: BAE39835.1.
AK167926 mRNA. Translation: BAE39931.1.
AK168271 mRNA. Translation: BAE40217.1.
AK169123 mRNA. Translation: BAE40903.1.
AK169210 mRNA. Translation: BAE40982.1.
AK169295 mRNA. Translation: BAE41051.1.
CR974451 Genomic DNA. Translation: CAO77890.1.
BC003825 mRNA. Translation: AAH03825.1.
M28732 mRNA. Translation: AAA40510.1.
PIRE25437.
RefSeqNP_035785.1. NM_011655.5.
UniGeneMm.273538.
Mm.472638.

3D structure databases

ProteinModelPortalP99024.
SMRP99024. Positions 2-427.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204381. 28 interactions.
IntActP99024. 32 interactions.
MINTMINT-1869561.

Chemistry

BindingDBP99024.

PTM databases

PhosphoSiteP99024.

2D gel databases

REPRODUCTION-2DPAGEIPI00117352.
P99024.
SWISS-2DPAGEP99024.

Proteomic databases

PRIDEP99024.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000001566; ENSMUSP00000001566; ENSMUSG00000001525.
GeneID22154.
KEGGmmu:22154.
UCSCuc008ciq.2. mouse.

Organism-specific databases

CTD22154.
MGIMGI:107812. Tubb5.

Phylogenomic databases

GeneTreeENSGT00750000117394.
HOVERGENHBG000089.
InParanoidB1B178.
KOK07375.
OMAELDYEDE.
OrthoDBEOG71ZP1H.
PhylomeDBP99024.
TreeFamTF300298.

Enzyme and pathway databases

ReactomeREACT_17056. Cooperation of Prefoldin and TriC/CCT in actin and tubulin folding.
REACT_93132. Metabolism of proteins.

Gene expression databases

ArrayExpressP99024.
BgeeP99024.
CleanExMM_TUBB5.
GenevestigatorP99024.

Family and domain databases

Gene3D1.10.287.600. 1 hit.
3.30.1330.20. 1 hit.
3.40.50.1440. 1 hit.
InterProIPR013838. Beta-tubulin_BS.
IPR002453. Beta_tubulin.
IPR008280. Tub_FtsZ_C.
IPR000217. Tubulin.
IPR018316. Tubulin/FtsZ_2-layer-sand-dom.
IPR023123. Tubulin_C.
IPR017975. Tubulin_CS.
IPR003008. Tubulin_FtsZ_GTPase.
[Graphical view]
PANTHERPTHR11588. PTHR11588. 1 hit.
PfamPF00091. Tubulin. 1 hit.
PF03953. Tubulin_C. 1 hit.
[Graphical view]
PRINTSPR01163. BETATUBULIN.
PR01161. TUBULIN.
SMARTSM00864. Tubulin. 1 hit.
SM00865. Tubulin_C. 1 hit.
[Graphical view]
SUPFAMSSF52490. SSF52490. 1 hit.
SSF55307. SSF55307. 1 hit.
PROSITEPS00227. TUBULIN. 1 hit.
PS00228. TUBULIN_B_AUTOREG. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSTUBB. mouse.
NextBio302074.
PROP99024.
SOURCESearch...

Entry information

Entry nameTBB5_MOUSE
AccessionPrimary (citable) accession number: P99024
Secondary accession number(s): B1B178 expand/collapse secondary AC list , P05218, Q3TFB6, Q3THH9, Q3TIL1, Q3UAV4, Q3UF52, Q8WUC1, Q9CY33
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: August 13, 1987
Last modified: April 16, 2014
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot